Modular binding domains in signal transduction proteins
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Proline-rich stretches have been implicated in mediating protein-protein interactions.
“which have been implicated in mediating protein-protein interactions (Cohen et al., 1995).”
From LRAD3, A Novel Low-Density Lipoprotein Receptor Family Member That Modulates Amyloid Precursor Protein Trafficking (2011) · cites this paper as Cohen et al., 1995
The PPPPY sequence in LRAD3 may also be recognized by molecules containing SH3 domains.
“Interestingly, not only does the PPPPY sequence in LRAD3 conform to the WW domain binding consensus, but this region may also be recognized by molecules containing src homology 3 (SH3) domains (Pawson and Scott, 1997; Pawson, 1995; Cohen et al., 1995).”
From LRAD3, A Novel Low-Density Lipoprotein Receptor Family Member That Modulates Amyloid Precursor Protein Trafficking (2011) · cites this paper as Cohen et al., 1995
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“There are four putative phosphorylation sites and two proline-rich stretches within the cytoplasmic domain, which have been implicated in mediating protein–protein interactions (Cohen et al., 1995).”
Background
- Authors
- Cohen, G. B., Ren, R., & Baltimore, D.
- Affiliations
- Massachusetts Institute of Technology (US)
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1995-01
- Volume
- 80
- Issue
- 2
- Pages
- 237-248
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2065033398
- Cited by
- 951
- References
- 0
- Citations by year
- 2026: 2 · 2025: 3 · 2024: 8 · 2023: 3 · 2022: 4 · 2021: 7 · 2020: 6 · 2019: 10 · 2018: 10 · 2017: 8 · 2016: 8 · 2015: 11 · 2014: 13 · 2013: 5 · 2012: 7
- FWCI
- 50.12
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- CaltechAUTHORS (California Institute of Technology) (submittedVersion)
- Funders
- Foundation for the National Institutes of Health
- Helen Hay Whitney Foundation
- National Cancer Institute (R01CA051462, 5RO1 CA51462-06)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- signal transduction, protein domains, second messengers, cyclic AMP, tyrosine kinase, Ras, signaling pathways, signal transducers
- MeSH terms
- Allosteric Regulation, Amino Acid Sequence, Animals, Binding Sites, Humans, Ligands, Models, Molecular, Molecular Sequence Data, Phosphoproteins, Phosphorylation, Protein-Tyrosine Kinases, Proteins, Second Messenger Systems, Signal Transduction, Sequence Homology, Amino Acid, Protein Structure, Secondary, ras Proteins
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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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